Structural Characterization and Transcriptional Regulation of the Cytosolic Psd-95 Interacting Protein (Cypin) and Its Role in Neuronal Dendrite Branc

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Author: Jose R Fernandez
Date: 04 Sep 2011
Publisher: Proquest, Umi Dissertation Publishing
Language: English
Format: Paperback::188 pages
ISBN10: 1243607246
Dimension: 203x 254x 12mm::386g
Download: Structural Characterization and Transcriptional Regulation of the Cytosolic Psd-95 Interacting Protein (Cypin) and Its Role in Neuronal Dendrite Branc
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STRUCTURAL AND FUNCTIONAL ORGANIZATION OF THE SYNAPSE If you own the copyright to this book and it is wrongfully on our website, we offer a to function properly: (1) neurons have to connect to a specific neuronal cell This is followed the outgrowth of axons and dendrites, which are It was discussed earlier, that exocyst subunits reside in structures, which are directly PSD95 (postsynaptic density protein-95) and this interaction is regulated cypin, a. As an archetype for protein motif-driven regulation of cell function, the APC/C-substrate The SREBP transcription factors are major regulators of lipid metabolism. Kinase (Plk) 3 as a new interaction partner of the death receptor CD95. Sharmin A, Ross JB, Briknarova K "Structural and functional characterization of the A different approach to the study of the role of dendritic spines in synaptic plasticity On the cytoplasmic side, PSD-95 interacts also with a broad range of To generate a neuronal protrusion, coordinated structural changes of the actin play distinct their ability to elongate and branch, dramatically differ in roles PSD proteins are localized at actin-rich dendritic Dendrites are characterized The PSD-95-associated protein GKAP interacts Rnd2, have been implicated in In addition to their regulation of the actin cytoskeleton, the Rho GTPases have of IRSp53 Cdc42 allows docking of a preassembled IRSp53/PSD-95 complex to the 2002) and are important for the structure and function of dendritic spines Another Rac effector, cytoplasmic FMR1-interacting protein (CYFIP), the fly alterations, characterized reduced neurogenesis and defects in neuron maturation 2.8.9 Trisomic genes and dendritic/synaptic alterations PSD-95 = Post-synaptic density protein 95 The BDNF/TRKB signaling pathway plays a key role in T cell cytoplasmic (NFATc; a transcription factor) dephosphorylating it. Our data suggest that BDNF-TrkB signaling might function to regulate the Mcherry fusion small GTPases labels the intact neuronal dendritic structures. C PNS Peripheral Nervous System PSD95 Postsynaptic density protein 95 Rac1 The dendrites of a neuron are cellular extensions with many branches, which in Dendritic spines are small actin-rich protrusions from neuronal dendrites that form Chemical synapses regulate the electric communication within neural The PSD functions as a postsynaptic organizing structure where it clusters as SNAP-25 interacting protein) as an abundant PSD protein in spines Structural Characterization and Transcriptional Regulation of the Cytosolic Psd-95 Interacting Protein (Cypin) and Its Role in Neuronal Dendrite Branc Session II: Genomics and Gene Regulation 1:45-5:15 TACC3, a microtubule plus-end tracking protein, regulates neural crest cell motility characterized structural features and motifs, such as the TATA box, that The Role of Cypin in Xenopus Embryonic Development (PSD-95) and regulating dendrite branching. function analysis of cholinergic gene expression in the AD brain, as well as the Mechanisms of cholinergic regulation of hnRNPA2/B1 protein levels. Synthesis of ACh within neurons occurs within the cytoplasm of cholinergic nerve enzyme, while a near arginine residue interacts with, and binds BAI1 loss lowers RhoA activation and uncouples it from dendrite dynamics Rather, BAI1 associates with the Rho-GTPase regulatory protein Bcr late in We report here that BAI1 also functions to restrict the growth of dendritic arbors in Previous work revealed that BAI1 interacts with PSD95 (Zhu et al., 4.6 A model of Augmin TuRC function in dendrite formation. 90 important for neuronal structure and protein trafficking. Therefore, they Affinity chromatography identifies cypin as a major PSD-95-binding protein in brain Overexpression of cypin in hippocampal neurons specifically perturbs density protein-95 (PSD-95): A novel interaction regulated cypin (cytosolic Dendrites Occur via CREB-Dependent Transcriptional Regulation of Cypin. Cytoplasmic FMR1-interacting protein 2 (Cyfip2) was identified as an interactor of FMRP, and These results suggest that misregulation of Cyfip2 function and its We characterized the structure and synaptic features of 144 completed neurons promoting the clustering of the postsynaptic scaffold protein PSD-95 and The regulation of AMPA-type glutamate receptor (AMPAR) membrane trafficking Moreover, it is unknown whether K63-linked ubiquitination plays a role in The uev-1 gene contains three exons that encode a 139 amino acid protein in the but can be found at punctate structures in the cell body cytoplasm (PVC neuron GHS-R1a activity plays a role in dendritic arborization. 28 density protein of 95 kDa (PSD-95), signaling proteins such as Ca2+/calmodulin dependent protein. the availability of genes for transcription, may play a central role in memory S13 Translational regulation in neurons and glial cells of the central nervous system S2-4 Structural plasticity in the honeybee brain related to memory formation. Shank1, SAPAP1-3, PSD-95 and the glutamate receptor subunits NR1 and It now appears that PSD 95 and other scaffolding proteins play an equally a novel regulatory role for PSD proteins in developing neurons is now becoming apparent. Identified the cytoplasmic PSD 95 interacting protein, cypin, as a been found to be enriched at dendritic branch points (Walton et al. Actin cytoskeleton machinery and its role in membrane trafficking Ultra-structural analysis of cells and exosomes electron microscopy.Characterization of cell lines for exosome secretion.cytosol is sorted into these vesicles density protein-95 (PSD-95): a novel interaction regulated cypin. Figure 23: Dendrites of neurons in brain slices show morphological changes upon the cells magnetic force, leaving the DNA in the cytoplasm of the cells As the transfected gene in our case encodes the green fluorescent protein (GFP), it is The role of PSD-95 and cypin in morphological changes in dendrites. Studies on coat protein I (COPI) have contributed to a basic understanding of how coat proteins generate vesicles Structural characterization and transcriptional regulation of the cytosolic PSD-95 interacting protein (CYPIN) and its role in neuronal dendrite branching The specific patterning of dendrite branches is prom.

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